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Q9UBU9

- NXF1_HUMAN

UniProt

Q9UBU9 - NXF1_HUMAN

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Protein
Nuclear RNA export factor 1
Gene
NXF1, TAP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway). The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of the TREX complex. ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1 heterodimer for export.3 Publications

GO - Molecular functioni

  1. mRNA binding Source: Ensembl
  2. nucleocytoplasmic transporter activity Source: Ensembl
  3. nucleotide binding Source: InterPro
  4. poly(A) RNA binding Source: UniProtKB
  5. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA export from nucleus Source: UniProtKB
  3. poly(A)+ mRNA export from nucleus Source: Ensembl
  4. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, mRNA transport, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
REACT_1835. Transport of Mature mRNA Derived from an Intronless Transcript.
REACT_405. Transport of the SLBP Dependant Mature mRNA.
REACT_424. Transport of the SLBP independent Mature mRNA.

Protein family/group databases

TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear RNA export factor 1
Alternative name(s):
Tip-associated protein
Tip-associating protein
mRNA export factor TAP
Gene namesi
Name:NXF1
Synonyms:TAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:8071. NXF1.

Subcellular locationi

Nucleusnucleoplasm. Nucleus speckle. Cytoplasm
Note: Localized predominantly in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex. Shuttles between the nucleus and the cytoplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. The association with the TREX complex seems to occur in regions surrounding nuclear speckles known as perispeckles.2 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nuclear inclusion body Source: Ensembl
  3. nuclear pore Source: Ensembl
  4. nuclear speck Source: UniProtKB
  5. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi71 – 711R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-78, A-81, A-82, A-89, A-91, A-97, A-98, A-100 and A-105. 1 Publication
Mutagenesisi78 – 781R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-81, A-82, A-89, A-91, A-97, A-98, A-100 and A-105. 1 Publication
Mutagenesisi81 – 811R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-82, A-89, A-91, A-97, A-98, A-100 and A-105. 1 Publication
Mutagenesisi82 – 821R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-89, A-91, A-97, A-98, A-100 and A-105. 1 Publication
Mutagenesisi89 – 891R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-91, A-97, A-98, A-100 and A-105. 1 Publication
Mutagenesisi91 – 911R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-97, A-98, A-100 and A-105. 1 Publication
Mutagenesisi97 – 971R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-91, A-98, A-100 and A-105. 1 Publication
Mutagenesisi98 – 981R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-91, A-97, A-100 and A-105. 1 Publication
Mutagenesisi100 – 1001R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-91, A-97, A-98 and A-105. 1 Publication
Mutagenesisi105 – 1051R → A: Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-91, A-97, A-98 and A-100. 1 Publication
Mutagenesisi306 – 3083ERE → AAA: Decreases the export of mRNAs from the nucleus.
Mutagenesisi383 – 3831L → R: Diminishes nuclear rim staining and 80% reduction in mRNA export activity; when associated with R-386. Complete loss of nuclear rim staining and mRNA export activity; when associated with R-386 and A-594. 1 Publication
Mutagenesisi386 – 3861L → R: Diminishes nuclear rim staining and 80% reduction in mRNA export activity; when associated with R-383. Complete loss of nuclear rim staining and mRNA export activity; when associated with R-383 and A-594. 1 Publication
Mutagenesisi399 – 3991D → A: 60% reduction in mRNA export activity. 1 Publication
Mutagenesisi450 – 4534LRFR → AAAA: Abolishes interaction with THOC5 and CHTOP. 2 Publications
Mutagenesisi453 – 4531R → A: Impairs intramolecular interaction between RBD and NTF2. 1 Publication
Mutagenesisi456 – 4594KHTR → AAAA: Abolishes interaction with THOC5 and CHTOP, no effect on interaction with NXT1; enhances intramolecular interaction between RBD and NTF2, reduces RNA binding and mRNA export. 2 Publications
Mutagenesisi456 – 4561K → D: Impairs intramolecular interaction between RBD and NTF2; when associated with D-459.
Mutagenesisi459 – 4591R → D: Impairs intramolecular interaction between RBD and NTF2; when associated with D-456.
Mutagenesisi482 – 4821D → R: 90% reduction in mRNA export activity. 1 Publication
Mutagenesisi518 – 5181I → R: 98% reduction in mRNA export activity. 1 Publication
Mutagenesisi521 – 5211P → Q: 35% reduction in mRNA export activity. 1 Publication
Mutagenesisi594 – 5941W → A: Suppresses FG-nucleoporin binding. Diminishes nuclear rim staining and 88% reduction in mRNA export activity. Complete loss of nuclear rim staining and mRNA export activity; when associated with R-383 and R-386. 1 Publication
Mutagenesisi595 – 5951D → R: Suppresses FG-nucleoporin binding.
Mutagenesisi617 – 6171F → A: Suppresses FG-nucleoporin binding. 1 Publication

Organism-specific databases

PharmGKBiPA31858.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 619618Nuclear RNA export factor 1
PRO_0000220529Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei126 – 1261Nitrated tyrosine By similarity

Keywords - PTMi

Acetylation, Nitration

Proteomic databases

MaxQBiQ9UBU9.
PaxDbiQ9UBU9.
PeptideAtlasiQ9UBU9.
PRIDEiQ9UBU9.

PTM databases

PhosphoSiteiQ9UBU9.

Expressioni

Tissue specificityi

Expressed ubiquitously.

Gene expression databases

ArrayExpressiQ9UBU9.
BgeeiQ9UBU9.
CleanExiHS_NXF1.
GenevestigatoriQ9UBU9.

Organism-specific databases

HPAiCAB016327.

Interactioni

Subunit structurei

Heterodimer with NXT1. Interacts (via NTF2 domain) with NXT1. The formation of NXF1-NXT1 heterodimers is required for the NXF1-mediated nuclear mRNA export. Interacts with NXT2, E1B-AP5, RAE1, ALYREF/THOC4, DDX39B, FYTTD1/UIF, EIF4A3, NUPL2 and with several nucleoporins. Interacts with THOC5 and CHTOP; in a mutually exclusive manner. Associates with the exon junction complex (EJC) and with the transcription/export (TREX) complex. Found in a mRNA complex with RENT3A and RENT3B. Interacts with Saimiriine herpesvirus 2 TIP protein. Interacts with human herpes virus 1 (HHV-1) ICP27 protein; this interaction allows efficient export of HHV-1 early and late transcripts.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P225756EBI-398874,EBI-866709From a different organism.
DDX3XO005715EBI-398874,EBI-353779
DHX9Q082118EBI-398874,EBI-352022
NUP62P371983EBI-398874,EBI-347978
NXT1Q9UKK62EBI-398874,EBI-301889
SRSF1Q079555EBI-398874,EBI-398920
SRSF3P841034EBI-398874,EBI-372557
SRSF7Q166294EBI-398874,EBI-398885
THRAP3Q9Y2W14EBI-398874,EBI-352039
UL54P102384EBI-398874,EBI-6883946From a different organism.

Protein-protein interaction databases

BioGridi115745. 94 interactions.
DIPiDIP-31789N.
IntActiQ9UBU9. 52 interactions.
MINTiMINT-121360.
STRINGi9606.ENSP00000294172.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi120 – 1245
Helixi127 – 1293
Helixi132 – 14110
Beta strandi143 – 1453
Beta strandi150 – 1556
Beta strandi158 – 1647
Helixi166 – 1749
Turni176 – 1783
Beta strandi190 – 1934
Helixi198 – 2014
Helixi206 – 21813
Turni222 – 2254
Beta strandi226 – 2283
Helixi232 – 2343
Helixi236 – 2405
Helixi250 – 26314
Beta strandi269 – 2713
Helixi281 – 2855
Helixi286 – 2894
Beta strandi295 – 2973
Helixi306 – 3127
Beta strandi318 – 3214
Helixi328 – 3303
Helixi334 – 34411
Beta strandi350 – 3534
Helixi381 – 39818
Helixi403 – 4086
Beta strandi410 – 41910
Helixi433 – 4364
Turni442 – 4443
Helixi448 – 4547
Beta strandi455 – 4584
Helixi459 – 4668
Beta strandi472 – 4743
Helixi476 – 4783
Beta strandi480 – 4867
Beta strandi491 – 50111
Turni505 – 5084
Beta strandi510 – 52112
Beta strandi525 – 53814
Helixi541 – 5488
Beta strandi553 – 5575
Helixi565 – 57814
Helixi582 – 59110
Turni592 – 5943
Helixi596 – 60813
Helixi614 – 6174

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FO1X-ray2.90A/B102-372[»]
1FT8X-ray3.15A/B/C/D/E102-372[»]
1GO5NMR-A551-619[»]
1JKGX-ray1.90B371-619[»]
1JN5X-ray2.80B371-619[»]
1KOHX-ray3.80A/B/C/D96-372[»]
1KOOX-ray3.80A/B/C/D96-372[»]
1OAIX-ray1.00A561-619[»]
2Z5KX-ray2.60B53-82[»]
2Z5MX-ray3.00B53-82[»]
3RW6X-ray2.30A/B96-362[»]
3RW7X-ray3.00A/B/C/D96-362[»]
ProteinModelPortaliQ9UBU9.
SMRiQ9UBU9. Positions 118-362, 371-619.

Miscellaneous databases

EvolutionaryTraceiQ9UBU9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini119 – 19880RRM
Add
BLAST
Repeati266 – 29126LRR 1
Add
BLAST
Repeati292 – 31524LRR 2
Add
BLAST
Repeati316 – 34328LRR 3
Add
BLAST
Repeati344 – 37128LRR 4
Add
BLAST
Domaini386 – 536151NTF2
Add
BLAST
Domaini565 – 61955TAP-C
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 198197Interaction with ALYREF/THOC4
Add
BLAST
Regioni2 – 118117RNA-binding (RBD)
Add
BLAST
Regioni2 – 6059Minor non-specific RNA-binding
Add
BLAST
Regioni61 – 11858Major non-specific RNA-binding
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi67 – 10034Nuclear localization signal
Add
BLAST
Motifi83 – 11028Nuclear export signal
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi551 – 56111Pro-rich
Add
BLAST

Domaini

The minimal CTE binding domain consists of an RNP-type RNA binding domain (RBD) and leucine-rich repeats.1 Publication
The nucleoporin binding domain consists of a NTF2 domain (also called NTF2-like domain) and a TAP-C domain (also called UBA-like domain). It has 2 nucleoporin-FG-repeats binding sites (one in the NTF2 and the other in the TAP-C domain) which contribute to nucleoporin association and act synergistically to export cellular mRNAs.1 Publication
The NTF2 domain is functional only in the presence of NXT1 and is essential for the export of mRNA from the nucleus. It inhibits RNA binding activity through an intramolecular interaction with the N-terminal RNA binding domain (RBD); the inhibition is removed by an association with the TREX complex, specifically involving ALYREF/THOC4 and THOC5.1 Publication
The TAP-C domain mediates direct interactions with nucleoporin-FG-repeats and is necessary and sufficient for localization of NXF1 to the nuclear rim. The conserved loop 594-NWD-596 of the TAP-C domain has a critical role in the interaction with nucleoporins.1 Publication
The leucine-rich repeats are essential for the export of mRNA from the nucleus.1 Publication
The RNA-binding domain is a non-canonical RNP-type domain.1 Publication

Sequence similaritiesi

Belongs to the NXF family.
Contains 1 NTF2 domain.
Contains 1 TAP-C domain.

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiNOG324438.
HOGENOMiHOG000236269.
HOVERGENiHBG013199.
InParanoidiQ9UBU9.
KOiK14284.
OMAiYAVYDSG.
OrthoDBiEOG7QZGB9.
PhylomeDBiQ9UBU9.
TreeFamiTF314566.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR001611. Leu-rich_rpt.
IPR002075. NTF2.
IPR018222. Nuclear_transport_factor_2_euk.
IPR012677. Nucleotide-bd_a/b_plait.
IPR005637. TAP_C_dom.
IPR015245. Tap_RNA-bd.
IPR003603. U2A'_phosphoprotein32A_C.
IPR009060. UBA-like.
[Graphical view]
PfamiPF00560. LRR_1. 1 hit.
PF02136. NTF2. 1 hit.
PF09162. Tap-RNA_bind. 1 hit.
PF03943. TAP_C. 1 hit.
[Graphical view]
ProDomiPD043466. Tap_RNA_bd. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00446. LRRcap. 1 hit.
SM00804. TAP_C. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
PROSITEiPS51450. LRR. 3 hits.
PS50177. NTF2_DOMAIN. 1 hit.
PS51281. TAP_C. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UBU9-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MADEGKSYSE HDDERVNFPQ RKKKGRGPFR WKYGEGNRRS GRGGSGIRSS    50
RLEEDDGDVA MSDAQDGPRV RYNPYTTRPN RRGDTWHDRD RIHVTVRRDR 100
APPERGGAGT SQDGTSKNWF KITIPYGRKY DKAWLLSMIQ SKCSVPFTPI 150
EFHYENTRAQ FFVEDASTAS ALKAVNYKIL DRENRRISII INSSAPPHTI 200
LNELKPEQVE QLKLIMSKRY DGSQQALDLK GLRSDPDLVA QNIDVVLNRR 250
SCMAATLRII EENIPELLSL NLSNNRLYRL DDMSSIVQKA PNLKILNLSG 300
NELKSERELD KIKGLKLEEL WLDGNSLCDT FRDQSTYISA IRERFPKLLR 350
LDGHELPPPI AFDVEAPTTL PPCKGSYFGT ENLKSLVLHF LQQYYAIYDS 400
GDRQGLLDAY HDGACCSLSI PFIPQNPARS SLAEYFKDSR NVKKLKDPTL 450
RFRLLKHTRL NVVAFLNELP KTQHDVNSFV VDISAQTSTL LCFSVNGVFK 500
EVDGKSRDSL RAFTRTFIAV PASNSGLCIV NDELFVRNAS SEEIQRAFAM 550
PAPTPSSSPV PTLSPEQQEM LQAFSTQSGM NLEWSQKCLQ DNNWDYTRSA 600
QAFTHLKAKG EIPEVAFMK 619
Length:619
Mass (Da):70,182
Last modified:May 1, 2000 - v1
Checksum:i338872AADA789FBF
GO
Isoform 2 (identifier: Q9UBU9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     339-356: SAIRERFPKLLRLDGHEL → RSVVACVSPPGDLHPLGG
     357-619: Missing.

Show »
Length:356
Mass (Da):40,476
Checksum:i470701F5324EC0B5
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei339 – 35618SAIRE…DGHEL → RSVVACVSPPGDLHPLGG in isoform 2.
VSP_041427Add
BLAST
Alternative sequencei357 – 619263Missing in isoform 2.
VSP_041428Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191W → C in AAB81111. 1 Publication
Sequence conflicti256 – 2561T → N in AAD20016. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ132712 mRNA. Translation: CAA10753.1.
AF112880 mRNA. Translation: AAD39102.1.
AF126246 mRNA. Translation: AAD20016.1.
AK304137 mRNA. Translation: BAG65031.1.
AK027192 mRNA. No translation available.
AP001160 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74105.1.
BC004904 mRNA. Translation: AAH04904.1.
BC028041 mRNA. Translation: AAH28041.1.
U80073 mRNA. Translation: AAB81111.1.
CCDSiCCDS44629.1. [Q9UBU9-2]
CCDS8037.1. [Q9UBU9-1]
RefSeqiNP_001074960.1. NM_001081491.1. [Q9UBU9-2]
NP_006353.2. NM_006362.4. [Q9UBU9-1]
UniGeneiHs.523739.
Hs.601546.

Genome annotation databases

EnsembliENST00000294172; ENSP00000294172; ENSG00000162231. [Q9UBU9-1]
ENST00000439713; ENSP00000408864; ENSG00000162231. [Q9UBU9-2]
ENST00000531709; ENSP00000453885; ENSG00000162231. [Q9UBU9-2]
ENST00000532297; ENSP00000436679; ENSG00000162231. [Q9UBU9-1]
GeneIDi10482.
KEGGihsa:10482.
UCSCiuc001nvf.1. human. [Q9UBU9-1]
uc001nvg.1. human. [Q9UBU9-2]

Polymorphism databases

DMDMi20139282.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ132712 mRNA. Translation: CAA10753.1 .
AF112880 mRNA. Translation: AAD39102.1 .
AF126246 mRNA. Translation: AAD20016.1 .
AK304137 mRNA. Translation: BAG65031.1 .
AK027192 mRNA. No translation available.
AP001160 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74105.1 .
BC004904 mRNA. Translation: AAH04904.1 .
BC028041 mRNA. Translation: AAH28041.1 .
U80073 mRNA. Translation: AAB81111.1 .
CCDSi CCDS44629.1. [Q9UBU9-2 ]
CCDS8037.1. [Q9UBU9-1 ]
RefSeqi NP_001074960.1. NM_001081491.1. [Q9UBU9-2 ]
NP_006353.2. NM_006362.4. [Q9UBU9-1 ]
UniGenei Hs.523739.
Hs.601546.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FO1 X-ray 2.90 A/B 102-372 [» ]
1FT8 X-ray 3.15 A/B/C/D/E 102-372 [» ]
1GO5 NMR - A 551-619 [» ]
1JKG X-ray 1.90 B 371-619 [» ]
1JN5 X-ray 2.80 B 371-619 [» ]
1KOH X-ray 3.80 A/B/C/D 96-372 [» ]
1KOO X-ray 3.80 A/B/C/D 96-372 [» ]
1OAI X-ray 1.00 A 561-619 [» ]
2Z5K X-ray 2.60 B 53-82 [» ]
2Z5M X-ray 3.00 B 53-82 [» ]
3RW6 X-ray 2.30 A/B 96-362 [» ]
3RW7 X-ray 3.00 A/B/C/D 96-362 [» ]
ProteinModelPortali Q9UBU9.
SMRi Q9UBU9. Positions 118-362, 371-619.
ModBasei Search...

Protein-protein interaction databases

BioGridi 115745. 94 interactions.
DIPi DIP-31789N.
IntActi Q9UBU9. 52 interactions.
MINTi MINT-121360.
STRINGi 9606.ENSP00000294172.

Protein family/group databases

TCDBi 3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSitei Q9UBU9.

Polymorphism databases

DMDMi 20139282.

Proteomic databases

MaxQBi Q9UBU9.
PaxDbi Q9UBU9.
PeptideAtlasi Q9UBU9.
PRIDEi Q9UBU9.

Protocols and materials databases

DNASUi 10482.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000294172 ; ENSP00000294172 ; ENSG00000162231 . [Q9UBU9-1 ]
ENST00000439713 ; ENSP00000408864 ; ENSG00000162231 . [Q9UBU9-2 ]
ENST00000531709 ; ENSP00000453885 ; ENSG00000162231 . [Q9UBU9-2 ]
ENST00000532297 ; ENSP00000436679 ; ENSG00000162231 . [Q9UBU9-1 ]
GeneIDi 10482.
KEGGi hsa:10482.
UCSCi uc001nvf.1. human. [Q9UBU9-1 ]
uc001nvg.1. human. [Q9UBU9-2 ]

Organism-specific databases

CTDi 10482.
GeneCardsi GC11M062559.
HGNCi HGNC:8071. NXF1.
HPAi CAB016327.
MIMi 602647. gene.
neXtProti NX_Q9UBU9.
PharmGKBi PA31858.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG324438.
HOGENOMi HOG000236269.
HOVERGENi HBG013199.
InParanoidi Q9UBU9.
KOi K14284.
OMAi YAVYDSG.
OrthoDBi EOG7QZGB9.
PhylomeDBi Q9UBU9.
TreeFami TF314566.

Enzyme and pathway databases

Reactomei REACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
REACT_1835. Transport of Mature mRNA Derived from an Intronless Transcript.
REACT_405. Transport of the SLBP Dependant Mature mRNA.
REACT_424. Transport of the SLBP independent Mature mRNA.

Miscellaneous databases

ChiTaRSi NXF1. human.
EvolutionaryTracei Q9UBU9.
GeneWikii NXF1.
GenomeRNAii 10482.
NextBioi 39766.
PROi Q9UBU9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UBU9.
Bgeei Q9UBU9.
CleanExi HS_NXF1.
Genevestigatori Q9UBU9.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR001611. Leu-rich_rpt.
IPR002075. NTF2.
IPR018222. Nuclear_transport_factor_2_euk.
IPR012677. Nucleotide-bd_a/b_plait.
IPR005637. TAP_C_dom.
IPR015245. Tap_RNA-bd.
IPR003603. U2A'_phosphoprotein32A_C.
IPR009060. UBA-like.
[Graphical view ]
Pfami PF00560. LRR_1. 1 hit.
PF02136. NTF2. 1 hit.
PF09162. Tap-RNA_bind. 1 hit.
PF03943. TAP_C. 1 hit.
[Graphical view ]
ProDomi PD043466. Tap_RNA_bd. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00446. LRRcap. 1 hit.
SM00804. TAP_C. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
PROSITEi PS51450. LRR. 3 hits.
PS50177. NTF2_DOMAIN. 1 hit.
PS51281. TAP_C. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "TAP binds to the constitutive transport element (CTE) through a novel RNA-binding motif that is sufficient to promote CTE-dependent RNA export from the nucleus."
    Braun I.C., Rohrbach E., Schmitt C., Izaurralde E.
    EMBO J. 18:1953-1965(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS.
    Tissue: Cervix carcinoma.
  2. "The human Tap protein is a nuclear mRNA export factor that contains novel RNA-binding and nucleocytoplasmic transport sequences."
    Kang Y., Cullen B.R.
    Genes Dev. 13:1126-1139(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Identification of novel import and export signals of human TAP, the protein that binds to the constitutive transport element of the type D retrovirus mRNAs."
    Bear J., Tan W., Zolotukhin A.S., Tabernero C., Hudson E.A., Felber B.K.
    Mol. Cell. Biol. 19:6306-6317(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Lung and Trachea.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain and Placenta.
  8. "Tap: a novel cellular protein that interacts with tip of herpesvirus saimiri and induces lymphocyte aggregation."
    Yoon D.-W., Lee H., Seol W., DeMaria M., Rosenzweig M., Jung J.U.
    Immunity 6:571-582(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 61-619, INTERACTION WITH SAIMIRIINE HERPESVIRUS 2 TIP.
    Tissue: Lymphocyte.
  9. "TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus."
    Grueter P., Tabernero C., von Kobbe C., Schmitt C., Saavedra C., Bachi A., Wilm M., Felber B.K., Izaurralde E.
    Mol. Cell 1:649-659(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human."
    Katahira J., Straesser K., Podtelejnikov A., Mann M., Jung J.U., Hurt E.
    EMBO J. 18:2593-2609(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NUPL2.
  11. "Overexpression of TAP/p15 heterodimers bypasses nuclear retention and stimulates nuclear mRNA export."
    Braun I.C., Herold A., Rode M., Conti E., Izaurralde E.
    J. Biol. Chem. 276:20536-20543(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  12. "The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates."
    Bachi A., Braun I.C., Rodrigues J.P., Pante N., Ribbeck K., von Kobbe C., Kutay U., Wilm M., Goerlich D., Carmo-Fonseca M., Izaurralde E.
    RNA 6:136-158(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  13. "Prediction of structural domains of TAP reveals details of its interaction with p15 and nucleoporins."
    Suyama M., Doerks T., Braun I.C., Sattler M., Izaurralde E., Bork P.
    EMBO Rep. 1:53-58(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  14. "Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex."
    Kataoka N., Diem M.D., Kim V.N., Yong J., Dreyfuss G.
    EMBO J. 20:6424-6433(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ALYREF/THOC4 AND THE EXON JUNCTION COMPLEX.
  15. "Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex."
    Kim V.N., Kataoka N., Dreyfuss G.
    Science 293:1832-1836(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH UPF3A AND UPF3B.
  16. "Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1."
    Lykke-Andersen J., Shu M.-D., Steitz J.A.
    Science 293:1836-1839(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A POST-SPLICING COMPLEX WITH RBM8A; UPF1; UPF2; UPF3A; UPF3B AND RNPS1.
  17. "eIF4A3 is a novel component of the exon junction complex."
    Chan C.C., Dostie J., Diem M.D., Feng W., Mann M., Rappsilber J., Dreyfuss G.
    RNA 10:200-209(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF4A3 AND ALYREF/THOC4.
  18. "Mutually exclusive interactions drive handover of mRNA from export adaptors to TAP."
    Hautbergue G.M., Hung M.L., Golovanov A.P., Lian L.Y., Wilson S.A.
    Proc. Natl. Acad. Sci. U.S.A. 105:5154-5159(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-71; ARG-78; ARG-81; ARG-82; ARG-89; ARG-91; ARG-97; ARG-98; ARG-100 AND ARG-105.
  19. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  20. "UIF, a new mRNA export adaptor that works together with REF/ALY, requires FACT for recruitment to mRNA."
    Hautbergue G.M., Hung M.L., Walsh M.J., Snijders A.P., Chang C.T., Jones R., Ponting C.P., Dickman M.J., Wilson S.A.
    Curr. Biol. 19:1918-1924(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FYTTD1.
  21. "Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA."
    Katahira J., Inoue H., Hurt E., Yoneda Y.
    EMBO J. 28:556-567(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ALYREF/THOC4 AND THOC5.
  22. "Assembly and mobility of exon-exon junction complexes in living cells."
    Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P., Wachsmuth M.
    RNA 15:862-876(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  23. "The cellular RNA export receptor TAP/NXF1 is required for ICP27-mediated export of herpes simplex virus 1 RNA, but the TREX complex adaptor protein Aly/REF appears to be dispensable."
    Johnson L.A., Li L., Sandri-Goldin R.M.
    J. Virol. 83:6335-6346(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN HERPES VIRUS 1 ICP27.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: ASSOCIATION WITH THE TREX COMPLEX, RNA-BINDING, MUTAGENESIS OF ARG-453 AND 456-LYS--ARG-459.
  26. Cited for: INTERACTION WITH CHTOP; THOC5 AND ALYREF, MUTAGENESIS OF 450-LEU--ARG-453 AND 456-LYS--ARG-459.
  27. "Mapping interactions between mRNA export factors in living cells."
    Teng I.F., Wilson S.A.
    PLoS ONE 8:E67676-E67676(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CHTOP.
  28. "The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain."
    Liker E., Fernandez E., Izaurralde E., Conti E.
    EMBO J. 19:5587-5598(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 102-372.
  29. "Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor."
    Fribourg S., Braun I.C., Izaurralde E., Conti E.
    Mol. Cell 8:645-656(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NXT1, X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NXT1-FG-REPEAT, SUBUNIT, DOMAINS, MUTAGENESIS OF LEU-383; LEU-386; ASP-399; ASP-482; ILE-518; PRO-521 AND TRP-594.
  30. "Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution."
    Grant R.P., Neuhaus D., Stewart M.
    J. Mol. Biol. 326:849-858(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 561-619 IN COMPLEX WITH RANBP3.
  31. "Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1."
    Grant R.P., Hurt E., Neuhaus D., Stewart M.
    Nat. Struct. Biol. 9:247-251(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 551-619, MUTAGENESIS OF PHE-617.

Entry informationi

Entry nameiNXF1_HUMAN
AccessioniPrimary (citable) accession number: Q9UBU9
Secondary accession number(s): B4E269, Q99799, Q9UQL2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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